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首页> 外文期刊>Biochemistry >Structural Organization of the Fibrin(ogen) #alpha#C-Domain
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Structural Organization of the Fibrin(ogen) #alpha#C-Domain

机译：纤维蛋白（基因）＃alpha＃C-结构域的结构组织

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We hypotesized that the #alpha#C-domain of human fibrinogen (residues hA#alpha#221-610) and of other species consists of a compact COOH-terminal region (hA#alpha#392-610) and a flexible NH_2-terminal connector region (hA#alpha#21-391) which may contain some regular structure [Weisel and Medved (2001) Ann. N.Y. Acad. Sci. 936, 312-391]. To test this hypotesis, we expressed in E. coli recombinant fragments corresponding to the full-length human #alpha#224-568, bA#alpha#224-373, and bA#alpha#374-568(538), respectively, and tested their folding status by fluorescence spectroscopy, circular dichroism (CD), and differential scanning calorimetry (DSC). All three methods revealed heat-induced unfolding transitions in the full-length bA#alpha#224-568 and its two COOH-terminal fragments, indicating that the COOH-terminal portion of the bovine #alpha#C-domain is folded into a compact cooperative structure. Similar results wre obtained by CD and DSC with the full-length and the COOH-terminal h392-610 human fragments. The NH_2-terminal fragments of both species, b224-373 and h221-392, did not exhibit any sign of a compact structure. However, their heat capacity functions, CD spectra, and temperature dependence of ellipticity at 222 nm were typical for peptides in the extended helical poly(L-proline) type II conformation (PPII), suggesting that they contain this tye of regular structure. This is consistent with the presence of proline-rich tnadem repeats in the sequence of both bovine and human connector regions. These results indicate that both ovine and human fibrinogen #alpha#C-domains consist of a compact globular cooperative unit attached to the bulk of the molecule by an extended NH_2-terminal connector region with a PPII conformation.
机译：我们假设，人类纤维蛋白原的＃alpha＃C结构域（残基hA＃alpha＃221-610）和其他物种的＃alpha＃C结构域由紧密的COOH末端区域（hA＃alpha＃392-610）和灵活的NH_2末端组成连接区（hA＃alpha＃21-391）可能包含一些规则结构[Weisel and Medved（2001）Ann。纽约州立学院科学936，312-391]。为了测试该假设，我们在大肠杆菌重组片段中分别表达了与全长人＃alpha＃224-568，bA＃alpha＃224-373和bA＃alpha＃374-568（538）相对应的片段，并通过荧光光谱法，圆二色性（CD）和差示扫描量热法（DSC）测试了它们的折叠状态。所有这三种方法都揭示了在全长bA＃alpha＃224-568及其两个COOH末端片段中热诱导的解折叠转变，表明牛＃alpha＃C结构域的COOH末端部分被折叠成紧密的合作结构。 CD和DSC用全长和COOH末端的h392-610人类片段获得了相似的结果。两种物种b224-373和h221-392的NH_2末端片段均未显示出致密结构的任何迹象。但是，它们的热容量函数，CD光谱和222 nm椭圆度的温度依赖性对于扩展螺旋II型（L-脯氨酸）II型构象（PPII）的肽来说是典型的，表明它们包含这种规则结构的肽。这与牛和人连接区的序列中富含脯氨酸的tnadem重复序列一致。这些结果表明，绵羊和人纤维蛋白原＃alpha＃C结构域均由紧密的球状协作单元组成，该球形协作单元通过具有PPII构象的扩展的NH_2末端连接区与分子的大部分相连。

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